| Project/Area Number |
62560101
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| Research Category |
Grant-in-Aid for General Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Research Field |
発酵・醸造
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| Research Institution | Kyoto University |
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Principal Investigator |
YANO Toshihiro (1988) Research Officer, Faculty of Agriculture, Kyoto University, 農学部, 教務職員 (30135553)
立木 隆 (1987) 京都大学, 農学部, 助手 (60026573)
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| Co-Investigator(Kenkyū-buntansha) |
TACHIKI Takashi Associate Professor, Faculty of Science and Engineering, Ritsumeikan University, 理工学部, 助教授 (60026573)
矢野 俊博 京都大学, 農学部, 教務職員 (30135553)
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| Project Period (FY) |
1987 – 1988
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| Project Status |
Completed (Fiscal Year 1988)
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| Budget Amount *help |
¥1,800,000 (Direct Cost: ¥1,800,000)
Fiscal Year 1988: ¥200,000 (Direct Cost: ¥200,000)
Fiscal Year 1987: ¥1,600,000 (Direct Cost: ¥1,600,000)
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| Keywords | Bifidobacteria / Enzymatic synthesis of oligosaccharides assimilable by bifidobacteria / Glutamate dehydrogenase / Glutamine synthetase / -D-Fucosylmannitol / -D-Glucosidase I / 特異的資化糖の酵素合成 / βーDグルコシダーゼI / アンモニア代謝 / 糖質代謝 |
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| Research Abstract |
1. Bifidobacterial enzymes participating in ammonia metabolism.
(1) Inactivation of glutamine synthetase (GS) in bifidobacteria was caused by enzymatic adenylylation of GS protein, and the adenylylation enzyme of bifidobacterium pseudolongum was characterized. The changes in the properties of the GS-reactions after the action of the enzyme were different from the findings obtained with enterobacteria but similar to those in a few species of actinomycetes.
(2) Glutamate dehydrogenases (GDHs) were purified from some bifidobacteria. Their enzymatic properties indicated that the enzymes catalyze reductive amination pysiologically rather than oxidative deamination, and suggested that they play some important role in ammonia metabolism together with GS.
(3) Analyses of variation of ammonia concentration in feces of a breast-fed infant suggested that bifidobacterial cells and GS might be concerned with elimination of ammonia in the lower intestines.
2. Properties and utilization of oligosaccharid
… More
e-hydrolyzing enzymes of bifidobacteria.
(1) A simple method was established for prepartion of a new -D-glucosidase ( -D-glucosid-ase I) from bifidobacterium breve 203, which has desirable properties for practical use.
(2) -D-glucosidase I hydrolyzed not only p-nitrophenyl (p-NP) -D-glucoside but also p-BP -D-fucoside and, furtheremore, transferred -D-fucosyl moiety to other sugars or sugar derivatives. By use of the enzyme, -D-fucosylglucose was synthesized in the mixture containing glucose as an acceptor with a yield of 52 % based on -D-fucosyl donor (p-NP -D-fucoside). The product consisted of four isomers ( 1-2, 1-3, 1,4 and 1-6), and it suppoeted specifically bifidobacterial growth. -D-fucosylmannitol was synthesized similarly with a yield of 45 %. It contained at least two isomers, however, their chemical structures and assimilability by bifidobacteria were not revealed in this study.
Formation of new substance was confirmed in reaction mixture containing maltose, xylose, glycerol or sorbitol as an acceptor. Less
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